Abstract
The initial contact of pathogens with host cells is usually mediated by their adhesion to glycan structures present on the cell surface in order to enable infection. Furthermore, glycans play important roles in the modulation of the host immune responses to infection. Understanding the carbohydrate-pathogen interactions are of importance for the development of novel and efficient strategies to either prevent, or interfere with pathogenic infection. Synthetic glycopeptides and mimetics thereof are capable of imitating the multivalent display of carbohydrates at the cell surface, which have become an important objective of research over the last decade. Glycopeptide based constructs may function as vaccines or anti-adhesive agents that interfere with the ability of pathogens to adhere to the host cell glycans and thus possess the potential to improve or replace treatments that suffer from resistance. Additionally, synthetic glycopeptides are used as tools for epitope mapping of antibodies directed against structures present on various pathogens and have become important to improve serodiagnostic methods and to develop novel epitope-based vaccines. This review will provide an overview of the most recent advances in the synthesis and application of glycopeptides and glycopeptide mimetics exhibiting a peptide-like backbone in glycobiology.
Highlights
Many human proteins are co- or post-translationally modified by mono- or oligosaccharides.Among a number of post-translational modifications, glycosylation is the most abundant form and it has been predicted that nearly 50% of all human proteins are glycosylated
For this reason, neutralizing antibodies that are directed to the glycopeptide epitopes of the viral glycoprotein could be of particular interest for vaccine development
While comparable binding to the mono, bi, and trivalent V3 glycopeptides was observed of antisera induced by the monovalent vaccine construct, the antisera induced by the trivalent vaccine construct showed up to 16-fold stronger binding to the multivalent glycopeptides
Summary
Many human proteins are co- or post-translationally modified by mono- or oligosaccharides. Among a number of post-translational modifications, glycosylation is the most abundant form and it has been predicted that nearly 50% of all human proteins are glycosylated Due to their complexity and structural diversity, carbohydrates and glycoconjugates play crucial roles in many key biological processes. Anti-adhesive agents that interfere with the ability of pathogens to adhere to the host cells may represents an attractive approach to fight infectious diseases [7] Inhibition of these host-pathogen interactions would be therapeutically significant, the development of effective inhibitors is demanding due to the structural diversity of glycans which includes the configuration, anomeric linkage, ring modification, hydroxyl group masking, charge, hydrophilicity, branching, and conformational properties. Synthetic glycopeptides have become important tools to characterize antibody binding signatures towards glycan and glycopeptide structures, which are present on various pathogens, and are useful to improve serodiagnostic methods and to develop novel epitope-based vaccines
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